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| - | [[Image:1bm8.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1bm8| PDB=1bm8 | SCENE= }} | | {{STRUCTURE_1bm8| PDB=1bm8 | SCENE= }} |
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| - | '''DNA-BINDING DOMAIN OF MBP1'''
| + | ===DNA-BINDING DOMAIN OF MBP1=== |
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| - | ==Overview==
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| - | BACKGROUND: During the cell cycle, cells progress through four distinct phases, G1, S, G2 and M; transcriptional controls play an important role at the transition between these phases. MCB-binding factor (MBF), a transcription factor from budding yeast, binds to the so-called MCB (MluI cell-cycle box) elements found in the promoters of many DNA synthesis genes, and activates the transcription of those at the G1-->S phase transition. MBF is comprised of two proteins, Mbp1 and Swi6. RESULTS: The three-dimensional structure of the N-terminal DNA-binding domain of Mbp1 has been determined by multiwavelength anomalous diffraction from crystals of the selenomethionyl variant of the protein. The structure is composed of a six-stranded beta sheet interspersed with two pairs of alpha helices. The most conserved core region among Mbp1-related transcription factors folds into a central helix-turn-helix motif with a short N-terminal beta strand and a C-terminal beta hairpin. CONCLUSIONS: Despite little sequence similarity, the structure within the core region of the Mbp1 N-terminal domain exhibits a similar fold to that of the DNA-binding domains of other proteins, such as hepatocyte nuclear factor-3gamma and histone H5 from eukaryotes, and the prokaryotic catabolite gene activator. However, the structure outside the core region defines Mbp1 as a larger entity with substructures that stabilize and display the helix-turn-helix motif.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_9083114}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 9083114 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_9083114}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Multiwavelength anomalous diffraction]] | | [[Category: Multiwavelength anomalous diffraction]] |
| | [[Category: Transcription factor]] | | [[Category: Transcription factor]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:41:33 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:22:42 2008'' |
Revision as of 16:22, 30 June 2008
Template:STRUCTURE 1bm8
DNA-BINDING DOMAIN OF MBP1
Template:ABSTRACT PUBMED 9083114
About this Structure
1BM8 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Crystal structure of the DNA-binding domain of Mbp1, a transcription factor important in cell-cycle control of DNA synthesis., Xu RM, Koch C, Liu Y, Horton JR, Knapp D, Nasmyth K, Cheng X, Structure. 1997 Mar 15;5(3):349-58. PMID:9083114
Page seeded by OCA on Mon Jun 30 19:22:42 2008
